Zaki Athraa J, Hartley Andrew M, Reddington Samuel C, Thomas Suzanne K, Watson Peter, Hayes Anthony, Moskalenko Andy V, Craciun Monica F, Macdonald J Emyr, Jones D Dafydd, Elliott Martin
School of Physics and Astronomy, Cardiff University Cardiff CF24 3AA UK
School of Biosciences, Cardiff University CF10 3AX UK
RSC Adv. 2018 Feb 5;8(11):5768-5775. doi: 10.1039/c7ra11166e. eCollection 2018 Feb 2.
We have created modified protein variants by introducing a non-canonical amino acid -azido-l-phenylalanine (azF) into defined positions for photochemically-induced covalent attachment to graphene. Attachment of GFP, TEM and cyt proteins was verified through a combination of atomic force and scanning tunnelling microscopy, resistance measurements, Raman data and fluorescence measurements. This method can in principle be extended to any protein which can be engineered in this way without adversely affecting its structural stability.
我们通过将一种非标准氨基酸——叠氮基-L-苯丙氨酸(azF)引入特定位置,以实现光化学诱导的与石墨烯的共价连接,从而创建了修饰后的蛋白质变体。通过原子力显微镜、扫描隧道显微镜、电阻测量、拉曼数据和荧光测量等多种手段,验证了绿色荧光蛋白(GFP)、透射电子显微镜(TEM)蛋白和细胞蛋白的连接情况。原则上,这种方法可以扩展到任何能够以这种方式进行工程改造且不会对其结构稳定性产生不利影响的蛋白质。